We propose to investigate certain enzymatic reactions in the degradation of L-beta-lysine by extracts of Pseudomonas B4. In particular, we plan to investigate the mechanism of the conversion of 4-acetamidobutyryl CoA to acetate, 4-aminobutyrate and CoA by an enzyme that has activities of both a thiolesterase and a deacetylase. Secondly, we propose to study the enzymatic reactions involved in the degradation of 3,5-diaminohexanoate by the aerobib Brevibacterium L5 to see how this process differs from that catalyzed by extracts of the anaerobic lysine-fermenting clostridia we have studies previously. We shall concentrate our efforts on the enzymes responsible for the degradation of 3-keto-5-aminohexanoate which was previously shown to be an intermediate in this system.